Cited by 988Antimicrobial Peptides and ActivitiesS100 Proteins and AnnexinsImmune Response and Inflammation

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Cathelicidins, multifunctional peptides of the innate immunity

Zanetti, Margherita·2004·Journal of Leukocyte Biology

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Abstract

Cathelicidins comprise a family of mammalian proteins containing a C-terminal cationic antimicrobial domain that becomes active after being freed from the N-terminal cathelin portion of the holoprotein. Many other members of this family have been identified since the first cathelicidin sequences were reported 10 years ago. The mature peptides generally show a wide spectrum of antimicrobial activity and, more recently, some of them have also been found to exert other biological activities. The human cathelicidin peptide LL-37 is chemotactic for neutrophils, monocytes, mast cells, and T cells; induces degranulation of mast cells; alters transcriptional responses in macrophages; stimulates wound vascularization and re-epithelialization of healing skin. The porcine PR-39 has also been involved in a variety of processes, including promotion of wound repair, induction of angiogenesis, neutrophils chemotaxis, and inhibition of the phagocyte NADPH oxidase activity, whereas the bovine BMAP-28 induces apoptosis in transformed cell lines and activated lymphocytes and may thus help with clearance of unwanted cells at inflammation sites. These multiple actions provide evidence for active participation of cathelicidin peptides in the regulation of the antimicrobial host defenses.

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Ong, P. Y., Ohtake, T., Brandt, C., Strickland, I., Boguniewicz, M., Ganz, T., Gallo, R. L., & Leung, D. Y. M. (2002) · New England Journal of Medicine · doi:10.1056/nejmoa021481 · Cited by 1,960
Amphipathic, α-helical antimicrobial peptides
Tossi, A., Sandri, L., & Giangaspero, A. (2000) · Biopolymers · doi:10.1002/1097-0282(2000)55:1 · Cited by 1,273
Self-citation
Ll-37, the Neutrophil Granule–And Epithelial Cell–Derived Cathelicidin, Utilizes Formyl Peptide Receptor–Like 1 (Fprl1) as a Receptor to Chemoattract Human Peripheral Blood Neutrophils, Monocytes, and T Cells
Yang, D., Chen, Q., Schmidt, A. P., Anderson, G. M., Wang, J., Wooters, J., Oppenheim, J. J., & Chertov, O. (2000) · The Journal of Experimental Medicine · doi:10.1084/jem.192.7.1069 · Cited by 1,238
The role of cationic antimicrobial peptides in innate host defences
Hancock, R. E. W., & Diamond, G. (2000) · Trends in Microbiology · doi:10.1016/s0966-842x(00)01823-0 · Cited by 1,233
Innate antimicrobial peptide protects the skin from invasive bacterial infection
Nizet, V., Ohtake, T., Lauth, X., Trowbridge, J., Rudisill, J., Dorschner, R. A., Pestonjamasp, V., Piraino, J., Huttner, K., & Gallo, R. L. (2001) · Nature · doi:10.1038/35106587 · Cited by 1,198
Biology of the Syndecans: A Family of Transmembrane Heparan Sulfate Proteoglycans
Bernfield, M. R., Kokenyesi, R., Kato, M., Hinkes, M. T., Spring, J., Gallo, R. L., & Lose, E. J. (1992) · Annual Review of Cell Biology · doi:10.1146/annurev.cb.08.110192.002053 · Cited by 1,099
Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3
Sørensen, O. E., Follin, P., Johnsen, A. H., Calafat, J., Tjabringa, G. S., Hiemstra, P. S., & Borregaard, N. (2001) · Blood · doi:10.1182/blood.v97.12.3951 · Cited by 894
An angiogenic role for the human peptide antibiotic LL-37/hCAP-18
Koczulla, R., von Degenfeld, G., Kupatt, C., Krötz, F., Zahler, S., GLOE, T. R., Issbrücker, K., Unterberger, P., Zaiou, M., Lebherz, C., et al. (2003) · Journal of Clinical Investigation · doi:10.1172/jci17545 · Cited by 880
The Expression of the Gene Coding for the Antibacterial Peptide LL-37 Is Induced in Human Keratinocytes during Inflammatory Disorders
Frohm, M., Agerberth, B., Ahangari, G., Ståhle‐Bäckdahl, M., Lidén, S., Wigzell, H., & Gudmundsson, G. H. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.24.15258 · Cited by 803

Show all 126 references

Research works printed but not linked: 2

Strukelj, 1995, Molecular cloning and identification of a novel porcine cathelin-like antibacterial peptide precursor, Biol. Chem. Hoppe Seyler, 376, 507
Larrick, 1995, Human CAP18: a novel antimicrobial lipopolysaccharide-binding protein, Infect. Immun., 63, 1291, 10.1128/iai.63.4.1291-1297.1995 · DOI

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Authors: Zanetti, M.
Affiliations: University of Udine (IT)
Corresponding author: Zanetti, Margherita
Venue: Journal of Leukocyte Biology
Publisher: Oxford University Press (OUP)
Published: 2003-07-22
Volume: 75
Issue: 1
Pages: 39-48
ISSN: 0741-5400 (ISSN-L)
1938-3673
DOI: 10.1189/jlb.0403147
OpenAlex: W1983987058
Cited by: 988
References: 126
Citations by year: 2026: 14 · 2025: 16 · 2024: 38 · 2023: 27 · 2022: 42 · 2021: 35 · 2020: 51 · 2019: 42 · 2018: 51 · 2017: 35 · 2016: 49 · 2015: 48 · 2014: 58 · 2013: 61 · 2012: 44
FWCI: 4.97
Type: journal article
Language: en
Open access: closed
Licence: academic.oup.com/pages/standard-publication-reuse-rights (vor)
Locations: Journal of Leukocyte Biology (publishedVersion)
PubMed (publishedVersion)
Institutional Research Information System (University of Udine) (submittedVersion)
Funders: Dept. Biochemistry of the University of Trieste
Dept. Biomedical Sciences and Technology of the University of Udine
Italian Ministry for University and Research (P.R.I.N. Cofin. 2000 and 2002)
CNR (Agenzia 2000)
Topics: Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › S100 Proteins and Annexins
Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
Keywords: cathelicidin, innate immunity, antimicrobial peptides, LL-37, PR-39, neutrophil chemotaxis, mast cell degranulation, angiogenesis, wound healing, apoptosis, NADPH oxidase inhibition
MeSH terms: Animals, Blood Proteins, Cattle, Chemotaxis, Leukocyte, Humans, Immunity, Innate, Macrophages, Protein Precursors, Proteins, T-Lymphocytes, Antimicrobial Cationic Peptides

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Cathelicidins, multifunctional peptides of the innate immunity

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